ID   ECT_ACRMI               Reviewed;         400 AA.
AC   B3EWZ8;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   25-MAY-2022, entry version 18.
DE   RecName: Full=Ectin {ECO:0000303|PubMed:23765379};
DE   Flags: Precursor; Fragment;
OS   Acropora millepora (Staghorn coral) (Heteropora millepora).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Acroporidae; Acropora.
OX   NCBI_TaxID=45264;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA   Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA   Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT   "Whole transcriptome analysis of the coral Acropora millepora reveals
RT   complex responses to CO(2)-driven acidification during the initiation of
RT   calcification.";
RL   Mol. Ecol. 21:2440-2454(2012).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 292-323 AND 328-352, TISSUE SPECIFICITY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23765379; DOI=10.1093/molbev/mst109;
RA   Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA   Guichard N., Miller D.J., Marin F.;
RT   "The skeletal proteome of the coral Acropora millepora: the evolution of
RT   calcification by co-option and domain shuffling.";
RL   Mol. Biol. Evol. 30:2099-2112(2013).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:23765379}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-soluble
CC       organic matrix of the aragonitic skeleton (at protein level).
CC       {ECO:0000269|PubMed:23765379}.
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DR   EMBL; JR978035; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; B3EWZ8; -.
DR   SMR; B3EWZ8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   CDD; cd05382; CAP_GAPR1-like; 1.
DR   Gene3D; 2.20.100.10; -; 2.
DR   Gene3D; 3.40.33.10; -; 1.
DR   InterPro; IPR014044; CAP_domain.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   InterPro; IPR034113; SCP_GAPR1-like.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF00090; TSP_1; 2.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF55797; SSF55797; 1.
DR   SUPFAM; SSF82895; SSF82895; 2.
DR   PROSITE; PS50092; TSP1; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..>400
FT                   /note="Ectin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000429498"
FT   DOMAIN          106..161
FT                   /note="TSP type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          163..218
FT                   /note="TSP type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DOMAIN          256..362
FT                   /note="SCP"
FT                   /evidence="ECO:0000255"
FT   DISULFID        118..155
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        122..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        133..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        175..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        179..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   DISULFID        190..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT   NON_TER         400
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  43385 MW;  86F243041CA3C508 CRC64;
     MMQASFSICI LSFYLLSFCH GAPLPAFLRS VLSGNGMKEE SRVLKRSAPV MQDEIPVCAQ
     NQTDRYSSSS RLCRLVKDLG FCDFDDLYQT VLQSCPIGCG FCRVEDGNWS VWGAWSPCSA
     TCGDGQRSRS RSCTNPPPSG GGADCLGVSQ EIEDCNRRSC EGIGGWSNWG QWSACSESCN
     IGIQARTRTC TNPPPTIPEG ACEGFSFETQ ICSTSGCNVS ASVSTAAATT SPVSSTAQTQ
     IGPTVVSLTA KQQACLDAHN AKRAIHGSPP LEWDFTLAMN ADEWANELAV TRQLEHDPNI
     MNEGENLFKS AGALECVDAV ERWFLEGKDY DYEDDNKLDD DTSNFTQLVW RNTTRVGVAT
     VVEVVSEGSV ETYIVARYTP PGNIEGKFEE NVIKPSAEAL